Phospholipase C‐γ, protein kinase C and Ca2+/calmodulin‐dependent protein kinase II are involved in platelet‐derived growth factor‐induced phosphorylation of Tiam1
- 16 June 1998
- journal article
- Published by Wiley in FEBS Letters
- Vol. 429 (3), 229-233
- https://doi.org/10.1016/s0014-5793(98)00566-3
Abstract
In Swiss 3T3 fibroblasts, the Rac1-specific guanine nucleotide exchange factor Tiam1 is phosphorylated by several different agonists. We show here that PDGF induces threonine phosphorylation of Tiam1 in a time- and dose-dependent manner. Tiam1 phosphorylation was significantly reduced by the selective protein kinase C inhibitor Ro-31-8220 and by KN93, an inhibitor of Ca2+/calmodulin-dependent protein kinase II. The Ca2+ chelator BAPTA/AM totally abrogated Tiam1 phosphorylation, indicating that Ca2+ is essential for this phosphorylation. Moreover, PDGF-stimulated Tiam1 phosphorylation was markedly reduced by 72±10% in PLC-γ1 deficient mouse fibroblasts, compared to wild-type cells, indicating that phosphoinositide phospholipase C is involved.Keywords
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